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N-acetylation of arylalkylmines (serotonin and tryptamine) in the crayfish brain.

Dubbels, R and Elofsson, Rolf LU (1989) In Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology 93. p.307-312
Abstract
1. The presence of N-acetyltransferase in the crayfish brain (Pacifastacus leniusculus) was investigated. The arylalkylamines tryptamine and 14C-serotonin, are acetylated by crayfish brain homogenates with the acetyl donors 3H-acetyl coenzyme A and N, S-diacetylcysteamine, respectively.

2. Resolution of serotonin metabolites by thin layer chromatography (chloroform/methanol/glacial acetic acid, 93 + 7 + 1 and ethyl acetate) revealed only one radioactive product (N-acetylserotonin, Rf 0.31) after enzymatic reaction. For example, melatonin and 5-hydroxyindole acetic acid could not be detected.

3. This was also confirmed by reversed phase high performance liquid chromatography indicating the absence of monoamine oxidase and... (More)
1. The presence of N-acetyltransferase in the crayfish brain (Pacifastacus leniusculus) was investigated. The arylalkylamines tryptamine and 14C-serotonin, are acetylated by crayfish brain homogenates with the acetyl donors 3H-acetyl coenzyme A and N, S-diacetylcysteamine, respectively.

2. Resolution of serotonin metabolites by thin layer chromatography (chloroform/methanol/glacial acetic acid, 93 + 7 + 1 and ethyl acetate) revealed only one radioactive product (N-acetylserotonin, Rf 0.31) after enzymatic reaction. For example, melatonin and 5-hydroxyindole acetic acid could not be detected.

3. This was also confirmed by reversed phase high performance liquid chromatography indicating the absence of monoamine oxidase and hydroxyindole-O-methyltransferase activity under the experimental conditions used.

4. Inhibitory studies with cystamine suggest the involvement of heat sensitive disulfide compounds in the regulation of crayfish brain-N-acetyltransferase.

5. N-acetylation seems to be a major pathway in the metabolism of biogenic amines in the crayfish central nervous system. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology
volume
93
pages
307 - 312
publisher
Elsevier
external identifiers
  • scopus:0024458159
ISSN
1532-0456
DOI
10.1016/0742-8413(89)90238-7
language
English
LU publication?
yes
id
176da897-f7ea-466a-bc82-be05260d4bc6
date added to LUP
2016-11-07 18:42:04
date last changed
2017-07-30 05:16:58
@article{176da897-f7ea-466a-bc82-be05260d4bc6,
  abstract     = {1. The presence of N-acetyltransferase in the crayfish brain (Pacifastacus leniusculus) was investigated. The arylalkylamines tryptamine and 14C-serotonin, are acetylated by crayfish brain homogenates with the acetyl donors 3H-acetyl coenzyme A and N, S-diacetylcysteamine, respectively.<br/><br/>2. Resolution of serotonin metabolites by thin layer chromatography (chloroform/methanol/glacial acetic acid, 93 + 7 + 1 and ethyl acetate) revealed only one radioactive product (N-acetylserotonin, Rf 0.31) after enzymatic reaction. For example, melatonin and 5-hydroxyindole acetic acid could not be detected.<br/><br/>3. This was also confirmed by reversed phase high performance liquid chromatography indicating the absence of monoamine oxidase and hydroxyindole-O-methyltransferase activity under the experimental conditions used.<br/><br/>4. Inhibitory studies with cystamine suggest the involvement of heat sensitive disulfide compounds in the regulation of crayfish brain-N-acetyltransferase.<br/><br/>5. N-acetylation seems to be a major pathway in the metabolism of biogenic amines in the crayfish central nervous system.},
  author       = {Dubbels, R and Elofsson, Rolf},
  issn         = {1532-0456},
  language     = {eng},
  pages        = {307--312},
  publisher    = {Elsevier},
  series       = {Comparative Biochemistry and Physiology Part - C: Toxicology and Pharmacology},
  title        = {N-acetylation of arylalkylmines (serotonin and tryptamine) in the crayfish brain.},
  url          = {http://dx.doi.org/10.1016/0742-8413(89)90238-7 },
  volume       = {93},
  year         = {1989},
}